The isolation of large molecular mass procyanidins from grain sorghum and their interaction with [14C]methyl bovine serum albumins.
1. Three protein-free procyanidin fractions with molecular masses of 4000, 8000 and 10,000-50,000 were isolated from a bird resistant sorghum grain. 2. The interaction between the largest procyanidin and 88 or 1% methylated bovine serum albumin (14C labelled) is stronger with the more methylated protein over a range of 0-2.75 ionic strength at pH 5. This indicates the involvement of apolar forces throughout the range though apolar forces were more pronounced from 0.7-2.75 ionic strength. 3. In the interaction between procyanidins of different molecular masses and 88% 14C-methylated bovine serum albumin the smaller procyanidins exhibited a more pronounced sigmoidal precipitation pattern than the larger with an increase in their concentrations.
McGrath
R M
RM
Department of Biochemistry, University of the Witwatersrand, South Africa.
Smith
A
A
D000818:Animals; D044946:Biflavonoids; D001667:Binding, Competitive; D002250:Carbon Radioisotopes; D002392:Catechin / Q000302:isolation & purification*; D002417:Cattle; D002850:Chromatography, Gel; D002523:Edible Grain / Q000032:analysis*; D008745:Methylation; D008970:Molecular Weight; D009994:Osmolar Concentration; D044945:Proanthocyanidins; D012710:Serum Albumin, Bovine / Q000378:metabolism*
D044946:Biflavonoids; D002250:Carbon Radioisotopes; D044945:Proanthocyanidins; D012710:Serum Albumin, Bovine; C017674:procyanidin; D002392:Catechin